Structure of PDB 2vxk Chain A Binding Site BS02

Receptor Information
>2vxk Chain A (length=165) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ENTPLFSPSLISPDVLAVLPADYTIRPLCRSDYKRGYLDVLRVLTTVGDI
NEEQWNSRYEWIRARSDEYYLLVVCDGEGRIVGTGSLVVERKFIHSLGMV
GHIEDIAVEKGQQGKKLGLRIIQALDYVAEKVGCYKTILDCSEANEGFYI
KCGFKRAGLEMAHYY
Ligand information
Ligand IDCOA
InChIInChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1
InChIKeyRGJOEKWQDUBAIZ-IBOSZNHHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(C)(CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[C@@H](O)C(=O)NCCC(=O)NCCS
OpenEye OEToolkits 1.5.0CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCS
ACDLabs 10.04O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
FormulaC21 H36 N7 O16 P3 S
NameCOENZYME A
ChEMBLCHEMBL1213327
DrugBankDB01992
ZINCZINC000008551087
PDB chain2vxk Chain A Residue 1193 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2vxk Structural and Kinetic Differences between Human and Aspergillus Fumigatus D-Glucosamine-6- Phosphate N-Acetyltransferase.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		Q138 G139 K141 G143 L144 A169 N170 F173 K176
Binding residue
(residue number reindexed from 1)		Q113 G114 K116 G118 L119 A144 N145 F148 K151
Annotation score3
Enzymatic activity
Enzyme Commision number 2.3.1.4: glucosamine-phosphate N-acetyltransferase.
Gene Ontology
Molecular Function
GO:0004343 glucosamine 6-phosphate N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006048 UDP-N-acetylglucosamine biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2vxk, PDBe:2vxk, PDBj:2vxk
PDBsum2vxk
PubMed18601654
UniProtQ4WCU5

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